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2V2C

The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM

Summary for 2V2C
Entry DOI10.2210/pdb2v2c/pdb
Related1AG1 1DKW 1IIG 1IIH 1KV5 1ML1 1MSS 1MTM 1TPD 1TPE 1TPF 1TRD 1TRI 1TSI 1TTI 1TTJ 2J24 2J27 2V0T 3TIM 4TIM 5TIM 6TIM
DescriptorTRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL, SULFATE ION, 2-PHOSPHOGLYCOLIC ACID, ... (4 entities in total)
Functional Keywordsisomerase, glycosome, tim-barrel, glycolysis, engineering, pentose shunt, point mutation, tim, 2pg, a178l, loop6, hinge, loop-6, enzyme, fatty acid biosynthesis, triosephosphate isomerase, gluconeogenesis, lipid synthesis, 2-phospho glycollate
Biological sourceTRYPANOSOMA BRUCEI BRUCEI
Cellular locationGlycosome: P04789
Total number of polymer chains1
Total formula weight27352.13
Authors
Alahuhta, M.,Casteleijn, M.G.,Neubauer, P.,Wierenga, R.K. (deposition date: 2007-06-05, release date: 2008-02-19, Last modification date: 2023-12-13)
Primary citationAlahuhta, M.,Casteleijn, M.G.,Neubauer, P.,Wierenga, R.K.
Structural Studies Show that the A178L Mutation in the C-Terminal Hinge of the Catalytic Loop-6 of Triosephosphate Isomerase (Tim) Induces a Closed-Like Conformation in Dimeric and Monomeric Tim.
Acta Crystallogr.,Sect.D, 64:178-, 2008
Cited by
PubMed: 18219118
DOI: 10.1107/S0907444907059021
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.89 Å)
Structure validation

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